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3ZHW

X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their Functional Implications

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005344molecular_functionoxygen carrier activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009505cellular_componentplant-type cell wall
A0009506cellular_componentplasmodesma
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0071456biological_processcellular response to hypoxia
B0001666biological_processresponse to hypoxia
B0005344molecular_functionoxygen carrier activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009505cellular_componentplant-type cell wall
B0009506cellular_componentplasmodesma
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0071456biological_processcellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 1163
ChainResidue
ALYS65
APHE114
AALA117
ALEU148
AHOH2022
AHOH2045
AHOH2071
BLEU158
BASN160
AHIS69
ASER72
AARG99
ALEU100
ASER103
AHIS104
ATYR107
AHIS113

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1902
ChainResidue
ALYS126
ATRP133
ALYS138
AHOH2049

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1904
ChainResidue
ALYS118
AVAL139
AGLY142
AGLN143
AASP146

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1905
ChainResidue
ALEU53
AARG54
ALYS65

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 1163
ChainResidue
BPHE50
BLYS65
BHIS69
BARG99
BLEU100
BSER103
BHIS104
BTYR107
BHIS113
BPHE114
BALA117
BVAL149

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1906
ChainResidue
BLYS126
BTRP133
BLYS138
BHOH2046
BHOH2056

Functional Information from PROSITE/UniProt
site_idPS00208
Number of Residues12
DetailsPLANT_GLOBIN Plant hemoglobins signature. NPkLkpHAmsvF
ChainResidueDetails
AASN63-PHE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS69
BHIS69

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS104
BHIS104

218853

PDB entries from 2024-04-24

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